These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Crystallization of succinyl-CoA synthetase from Escherichia coli.
    Author: Wolodko WT, James MN, Bridger WA.
    Journal: J Biol Chem; 1984 Apr 25; 259(8):5316-20. PubMed ID: 6371002.
    Abstract:
    Well formed, tetragonal prisms of succinyl-CoA synthetase from Escherichia coli have been crystallized at room temperature from ammonium sulfate and mixtures of sodium and potassium phosphates. A systematic survey of the conditions for crystallization of the enzyme has been carried out. This has shown the addition of a small amount of an organic solvent (acetone, 2-methyl-2,4-pentanediol, tert-butyl alcohol, or tertamyl alcohol) to the phosphate media and of CoA to the sulfate media to be beneficial in producing large, single crystals suitable for analysis by x-ray diffraction methods. Preliminary examination of precession photographs reveals that the crystals from phosphate media have a unit cell of symmetry P4222 with dimensions a = b = 94 A and c = 248 A. Evidence suggests that there may be only half of the (alpha beta)2 tetramer/asymmetric unit in these crystals. The crystals from ammonium sulfate media have unit cell dimensions of a = b = 99 A and c = 399 A, a space group of P4122 (P4322), and one tetramer/asymmetric unit. They diffract to a resolution of 3.4 A. Both crystal types have large solvent contents of about 65% of the unit cell volumes. A parameter called "quality index" is introduced to facilitate comparison of crystals grown under a variety of conditions with respect to their quality of x-ray diffraction.
    [Abstract] [Full Text] [Related] [New Search]